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Cell Biology

  1. James P. Gosling

Published Online: 15 SEP 2006

DOI: 10.1002/3527600906.mcb.200400088

Reviews in Cell Biology and Molecular Medicine

Reviews in Cell Biology and Molecular Medicine

How to Cite

Gosling, J. P. 2006. Immunoassays. Reviews in Cell Biology and Molecular Medicine. .

Author Information

  1. National University of Ireland, Department of Biochemistry, Galway, Ireland

Publication History

  1. Published Online: 15 SEP 2006


Specific, biologically related, intermolecular interaction is the basis of all “binding assays,” recombinant DNA procedures, and, accompanied by catalysis, of enzymatic analysis. “Binding assays,” also referred to by the term saturation analysis, depend on the “bio-recognition” of analytes by high affinity, specific binding proteins. In the last forty years “protein binding assays” have found so many applications in diverse areas of biochemical and chemical analysis that they now represent a standard analytical principle, like colorimetry or chromatography.

While there are many kinds of high affinity, specific binding proteins in nature (hormone receptors, for example), the special properties of antibodies have made them the most popular choice by far, for such methods. The term “immunoassay” applies to measurement procedures that use antibodies as specific binding reagents, as well as to assays that use antigens for the detection or quantification of specific antibodies. It is because of the extraordinary variety, specificity, and affinity of antibody–antigen binding reactions, that immunoassays are used for routine analyses and for research purposes throughout the biological and medical sciences.

Often an immunoassay procedure is chosen to measure a particular analyte because no other type of assay is technically feasible, which is true for specific antibodies, for most proteins and for many other complex biomolecules. But frequently, immunoassays are used because they match or exceed analytical and practical requirements and are more convenient and cost-effective than any alternative method.

When a broad perspective is adopted, it is clear that the history of immunotechnology as applied to the detection and quantitation of antigens did not begin with the invention of radioimmunoassay in the late 1950s. Rather, experimental immunologists have always used specific antibodies and “purified” antigens in their investigations, and major developments with respect to “immunoassay methodology” occurred when these were applied clinically and/or formulated to maximize their utility to clinical microbiologists, clinical chemists, and others. Table 1 lists some of the significant advances in this long history of the development of immunoassay methodology.


  • Automated;
  • Binding Affinity;
  • Classification;
  • Epitope;
  • Hapten;
  • Hybridoma;
  • Immunoglobulin Structure;
  • Interference;
  • Label;
  • Microarray;
  • Monoclonal Antibody;
  • Multiplexed;
  • Paratope;
  • Polyclonal Antibody;
  • Rapid Test Device;
  • Reagent-excess;
  • Reagent-limited;
  • Separation-free;
  • Solid Phase;
  • Standardization;
  • Structural Complementarity